Abstract
Recently, Rossman et al.1 have described the three-dimensional structure of a human rhinovirus. A possible host cell surface receptor binding site was identified with a cleft on each icosahedral face. Two highly conserved amino-acid sequences found in rhino-, polio-, and foot-and-mouth disease (FMD) viruses are located near the base of this site and could be important in maintaining its topology. We have prepared site-specific antibodies2,3 to two synthetic peptides which include these sequences. The antibodies bind to the predicted capsid proteins of rhinovirus and neutralize ˜60% of 48 rhinovirus serotypes tested. These results could provide a route to a rhinovirus vaccine effective against most of the numerous serotypes of this virus.
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McCray, J., Werner, G. Different rhinovirus serotypes neutralized by antipeptide antibodies. Nature 329, 736–738 (1987). https://doi.org/10.1038/329736a0
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DOI: https://doi.org/10.1038/329736a0
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